Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Subviral Agents01:29

Subviral Agents

Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Exon Recombination02:32

Exon Recombination

The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes. 
Exon shuffling follows “splice frame rules.” Each exon has three reading...
Viruses with RNA Genomes01:29

Viruses with RNA Genomes

RNA viruses are categorized into positive-strand, negative-strand, or double-stranded groups based on their genomic structure and replication mechanisms. This classification dictates how they exploit host cellular machinery for protein synthesis and replication. Some RNA viruses also utilize reverse transcription as part of their life cycle, further diversifying their replication strategies.Positive-Strand RNA VirusesPositive-strand RNA viruses have genomes that function directly as messenger...
Viral Mutations00:36

Viral Mutations

A mutation is a change in the sequence of bases of DNA or RNA in a genome. Some mutations occur during replication of the genome due to errors made by the polymerase enzymes that replicate DNA or RNA. Unlike DNA polymerase, RNA polymerase is prone to errors because it is not capable of “proofreading” its work. Viruses with RNA-based genomes, like HIV, therefore accrue mutations faster than viruses with DNA-based genomes. Because mutation and recombination provide the raw material for adaptive...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Anti-mGluR5 encephalitis: distinctive clinical features and antibody patterns in the Chinese population.

Frontiers in immunology·2026
Same author

Prion-like transmission and propagation of human β-amyloid to the bank vole rodent model.

Acta neuropathologica·2026
Same author

PrP<sup>C</sup>-facilitated cell signaling activates phospholipase Cɣ1 and triggers an Arc/Arg3.1 response in mouse and iPSC-derived human neurons.

Stem cell reports·2026
Same author

A Multidisciplinary Analytical Strategy for the Authentication and Quality Assessment of Bromelain in Dietary Supplements.

International journal of molecular sciences·2026
Same author

A single large-scale mitochondrial DNA deletion presenting as rapidly progressive dementia in a 35-year-old male.

NPJ dementia·2026
Same author

Multi-target approaches to prion disease drug discovery: a status update.

Expert opinion on drug discovery·2026
Same journal

PKM and the maintenance of memory.

F1000 biology reports·2013
Same journal

Cytokines in chronic respiratory diseases.

F1000 biology reports·2013
Same journal

Protein flexibility, not disorder, is intrinsic to molecular recognition.

F1000 biology reports·2013
Same journal

The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure.

F1000 biology reports·2013
Same journal

Is perceptual learning associated with changes in a sensory region?

F1000 biology reports·2012
Same journal

Molecular evolution and genetics of postzygotic reproductive isolation in plants.

F1000 biology reports·2012
See all related articles

Related Experiment Video

Updated: Jun 8, 2026

Protein Misfolding Cyclic Amplification of Prions
10:12

Protein Misfolding Cyclic Amplification of Prions

Published on: November 7, 2012

De novo prions.

Federico Benetti, Michael D Geschwind, Giuseppe Legname

    F1000 Biology Reports
    |October 16, 2010
    PubMed
    Summary
    This summary is machine-generated.

    Prions cause fatal neurodegenerative diseases through protein modification. Recent studies support the

    More Related Videos

    Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
    12:57

    Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

    Published on: January 8, 2015

    High-throughput Screening for Protein-based Inheritance in S. cerevisiae
    08:12

    High-throughput Screening for Protein-based Inheritance in S. cerevisiae

    Published on: August 8, 2017

    Related Experiment Videos

    Last Updated: Jun 8, 2026

    Protein Misfolding Cyclic Amplification of Prions
    10:12

    Protein Misfolding Cyclic Amplification of Prions

    Published on: November 7, 2012

    Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
    12:57

    Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

    Published on: January 8, 2015

    High-throughput Screening for Protein-based Inheritance in S. cerevisiae
    08:12

    High-throughput Screening for Protein-based Inheritance in S. cerevisiae

    Published on: August 8, 2017

    Area of Science:

    • Neuroscience
    • Biochemistry
    • Pathology

    Background:

    • Prions are misfolded proteins responsible for fatal neurodegenerative diseases.
    • These diseases manifest in sporadic, genetic, or acquired forms.
    • Prion diseases involve the conversion of normal cellular prion protein (PrP(C)) into infectious PrP(Sc) via post-translational modification.

    Purpose of the Study:

    • To explore the 'protein-only' hypothesis regarding prion generation.
    • To present recent in vivo and in vitro evidence supporting de novo prion formation.

    Main Methods:

    • Review of existing literature on prion diseases.
    • Analysis of recent experimental findings (in vivo and in vitro).

    Main Results:

    • Recent research strengthens the postulate that prions can be generated de novo.
    • Evidence supports the 'protein-only' hypothesis for prion propagation.

    Conclusions:

    • The 'protein-only' hypothesis is increasingly supported by experimental data.
    • Further research into prion formation mechanisms is warranted.